eF-site ID 1aui-A PDB Code 1aui Chain A click to enlarge Title HUMAN CALCINEURIN HETERODIMER Classification HYDROLASE Compound SERINE/THREONINE PHOSPHATASE 2B Source null (CANB1_HUMAN) Sequence A:  TDRVVKAVPFPPSHRLTAKEVFDNDGKPRVDILKAHLMKE GRLEESVALRIITEGASILRQEKNLLDIDAPVTVCGDIHG QFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYL WALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSER VYDACMDAFDCLPLAALMNQQFLCVHGGLSPEINTLDDIR KLDRFKEPPAYGPMCDILWSDPLEDFGNEKTQEHFTHNTV RGCSYFYSYPAVCEFLQHNNLLSILRAHEAQDAGYRMYRK SQTTGFPSLITIFSAPNYLDVYNNKAAVLKYENNVMNIRQ FNCSPHPYWLPNFMDVFTWSLPFVGEKVTEMLVNVLNICS SFEEAKGLDRINERMPPR Description Functional site 1) chain A residue 90 type sequence D description FE BINDING SITE. source : FEB 2) chain A residue 92 type sequence H description FE BINDING SITE. source : FEB 3) chain A residue 118 type sequence D description FE BINDING SITE. source : FEB 4) chain A residue 118 type sequence D description ZN BINDING SITE. source : ZNB 5) chain A residue 150 type sequence N description ZN BINDING SITE. source : ZNB 6) chain A residue 199 type sequence H description ZN BINDING SITE. source : ZNB 7) chain A residue 281 type sequence H description ZN BINDING SITE. source : ZNB 8) chain A residue 118 type sequence D description BINDING SITE FOR RESIDUE ZN A 522 source : AC5 9) chain A residue 150 type sequence N description BINDING SITE FOR RESIDUE ZN A 522 source : AC5 10) chain A residue 199 type sequence H description BINDING SITE FOR RESIDUE ZN A 522 source : AC5 11) chain A residue 281 type sequence H description BINDING SITE FOR RESIDUE ZN A 522 source : AC5 12) chain A residue 90 type sequence D description BINDING SITE FOR RESIDUE FE A 523 source : AC6 13) chain A residue 92 type sequence H description BINDING SITE FOR RESIDUE FE A 523 source : AC6 14) chain A residue 118 type sequence D description BINDING SITE FOR RESIDUE FE A 523 source : AC6 15) chain A residue 90 type catalytic sequence D description 406 source MCSA : MCSA1 16) chain A residue 92 type catalytic sequence H description 406 source MCSA : MCSA1 17) chain A residue 118 type catalytic sequence D description 406 source MCSA : MCSA1 18) chain A residue 121 type catalytic sequence D description 406 source MCSA : MCSA1 19) chain A residue 122 type catalytic sequence R description 406 source MCSA : MCSA1 20) chain A residue 150 type catalytic sequence N description 406 source MCSA : MCSA1 21) chain A residue 151 type catalytic sequence H description 406 source MCSA : MCSA1 22) chain A residue 199 type catalytic sequence H description 406 source MCSA : MCSA1 23) chain A residue 254 type catalytic sequence R description 406 source MCSA : MCSA1 24) chain A residue 281 type catalytic sequence H description 406 source MCSA : MCSA1 25) chain A residue 469 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P63329 source Swiss-Prot : SWS_FT_FI6 26) chain A residue 147-152 type prosite sequence LRGNHE description SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE source prosite : PS00125 27) chain A residue 281 type BINDING sequence H description BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE source Swiss-Prot : SWS_FT_FI2

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